ID   HPBP1_RAT               Reviewed;         357 AA.
AC   Q6IMX7; Q9JLF4;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Hsp70-binding protein 1;
DE            Short=HspBP1;
DE   AltName: Full=Heat shock protein-binding protein 1;
DE   AltName: Full=Hsp70-interacting protein 1;
GN   Name=Hspbp1; Synonyms=Hspbp;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=10786638; DOI=10.1016/s0167-4781(99)00238-9;
RA   Guerriero V. Jr., Raynes D.A.;
RT   "Isolation and characterization of isoforms of HspBP1, inhibitors of
RT   Hsp70.";
RL   Biochim. Biophys. Acta 1490:203-207(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Inhibits HSPA1A chaperone activity by changing the
CC       conformation of the ATP-binding domain of HSPA1A and interfering with
CC       ATP binding. Interferes with ubiquitination mediated by STUB1 and
CC       inhibits chaperone-assisted degradation of target proteins (By
CC       similarity). {ECO:0000250, ECO:0000269|PubMed:10786638}.
CC   -!- SUBUNIT: Interacts with the ATP-binding domain of HSPA1A. Detected in a
CC       ternary complex containing STUB1, HSPA1A and HSPBP1 (By similarity).
CC       Interacts with PGLYRP1; this interaction blocks the cytotoxic activity
CC       of the PGLYRP1-HSPA1A complex (By similarity). {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10786638}.
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DR   EMBL; AF187860; AAF35834.1; -; mRNA.
DR   EMBL; BC072541; AAH72541.1; -; mRNA.
DR   RefSeq; NP_640354.1; NM_139261.1.
DR   RefSeq; XP_006228310.1; XM_006228248.1.
DR   RefSeq; XP_006228311.1; XM_006228249.2.
DR   RefSeq; XP_006228312.1; XM_006228250.3.
DR   AlphaFoldDB; Q6IMX7; -.
DR   SMR; Q6IMX7; -.
DR   IntAct; Q6IMX7; 1.
DR   STRING; 10116.ENSRNOP00000024251; -.
DR   iPTMnet; Q6IMX7; -.
DR   PhosphoSitePlus; Q6IMX7; -.
DR   jPOST; Q6IMX7; -.
DR   PaxDb; Q6IMX7; -.
DR   PRIDE; Q6IMX7; -.
DR   Ensembl; ENSRNOT00000024251; ENSRNOP00000024251; ENSRNOG00000017795.
DR   GeneID; 246146; -.
DR   KEGG; rno:246146; -.
DR   UCSC; RGD:628677; rat.
DR   CTD; 23640; -.
DR   RGD; 628677; Hspbp1.
DR   eggNOG; KOG2160; Eukaryota.
DR   GeneTree; ENSGT00940000153909; -.
DR   HOGENOM; CLU_049387_0_1_1; -.
DR   InParanoid; Q6IMX7; -.
DR   OMA; CHVQSGL; -.
DR   OrthoDB; 1310125at2759; -.
DR   PhylomeDB; Q6IMX7; -.
DR   TreeFam; TF324307; -.
DR   PRO; PR:Q6IMX7; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000017795; Expressed in testis and 19 other tissues.
DR   Genevisible; Q6IMX7; RN.
DR   GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IBA:GO_Central.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:RGD.
DR   GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:RGD.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR013918; Nucleotide_exch_fac_Fes1.
DR   Pfam; PF08609; Fes1; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..357
FT                   /note="Hsp70-binding protein 1"
FT                   /id="PRO_0000084038"
FT   REPEAT          130..172
FT                   /note="ARM 1"
FT   REPEAT          175..215
FT                   /note="ARM 2"
FT   REPEAT          218..257
FT                   /note="ARM 3"
FT   REPEAT          260..299
FT                   /note="ARM 4"
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         349
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         354
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZL4"
FT   CONFLICT        205
FT                   /note="K -> N (in Ref. 1; AAF35834)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   357 AA;  39191 MW;  9DF1A7EE6E88AE7C CRC64;
     MADKGSGGSR LPLALPPASQ GCSSGSSGSS AGGSGNPRLP RNLQGLLQMA ITAGSEEPDP
     PPEPMSEERR QWLQEAMSAA FRGQREEVEQ MKNCLRVLSQ ATPPTAGEAE LATDQQEREG
     ALELLADLCE NMDNAADFCQ LSGMHLLVGR YLEAGAAGLR WRAAQLIGTC SQNVAAIQEQ
     VLGLGALRKL LRLLDRDSCD TVRVKALFAI SCLVREQEAG LLQFLRLDGF SVLMRAMQQQ
     VQKLKVKSAF LLQNLLVGHP EHKGTLCSMG MVQQLVALVR TEHSPFHEHV LGALCSLVTD
     FPQGVRECRE PELGLEELLR HRCQLLQQHE EYQEELEFCE KLLQTCFSSP TDDSMDR